ID F4B6L9_ACIHW Unreviewed; 410 AA.
AC F4B6L9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfideoxido reductase {ECO:0000313|EMBL:AEE93429.1};
GN OrderedLocusNames=Ahos_0541 {ECO:0000313|EMBL:AEE93429.1};
OS Acidianus hospitalis (strain W1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE93429.1, ECO:0000313|Proteomes:UP000008458};
RN [1] {ECO:0000313|EMBL:AEE93429.1, ECO:0000313|Proteomes:UP000008458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1 {ECO:0000313|EMBL:AEE93429.1,
RC ECO:0000313|Proteomes:UP000008458};
RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA She Q., Liu S.J., Garrett R.A.;
RT "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 15:487-497(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W1;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA Liu S.J., Garrett R.A.;
RT "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 0:0-0(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002535; AEE93429.1; -; Genomic_DNA.
DR RefSeq; WP_013775345.1; NC_015518.1.
DR AlphaFoldDB; F4B6L9; -.
DR STRING; 933801.Ahos_0541; -.
DR GeneID; 10599983; -.
DR KEGG; aho:Ahos_0541; -.
DR eggNOG; arCOG01068; Archaea.
DR HOGENOM; CLU_016755_0_3_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000008458; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 2..288
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 307..404
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 410 AA; 44795 MW; 5AF5863B7F7A6C1A CRC64;
MNITIIGSGP AGIYSAIASA KLGNKVKLVE KNDKLGGTCV LHGCIPSKAM LHPLFLKYFA
EETGRELNFS FSEIQKIAKN AVNRLSKGVE YMLESYGIEV IHGKAELRSG NIQVGGQTIP
SDKIIIATGT EKPQVEGTIA SDDLPYLDKE FSKVLVVGGG AGGVEYAWLL KMSGKDVSIV
EKSDNLLPYL DEDLKKAVTA YFKKIGIKLY LSSEITLGDK PRIGNEELPQ YDIILYTFGR
KPALDGFEEL PHEKWIKVDK RMYTGVNNIY AAGDITGTFT AHEAIHEGFV AGLNASGIEK
YYKPEAVPKV IYTEPQIAYV GNTKGKCVKI NMAEIPRAIA EGLTEGFLKV CVEGKKITGA
VAFSHDAENT ITLISTFINY GIEIDKAIDF IEPHPSYLEA VFEALLRLNS
//
